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Effect of thermosensitive matrix-phase transition on urease-catalyzed urea hydrolysis

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Abstract

Temperature dependencies of kinetic and equilibrium parameters of urea hydrolysis catalyzed by native urease and the urease immobilized in a thermosensitive poly-N-isopropylacrylamide gel have been studied. The swelling ratio of the collapsed urease-containing gel is shown to increase in the presence of urea. Below a lower critical solution temperature (LCST) of the polymer, the immobilized u reaseactually has thesame catalytic properties as the native enzyme. At temperatures above LCST, the observed catalytic activity of the immobilized enzyme depends chiefly not only on the thermoreversible matrix state, but also on gel water content.

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Abbreviations

E a :

activation energy, kJ/mol

K m :

Michaelis constant, M

V :

reaction rate, mM/min

V max :

maximum reaction rate, mM/min

V max.opf :

maximum reaction rate in a pH optimum of enzyme activity, mM/min

T :

temperature, K

t :

temperatue, °C

([NH2)2CO):

urea concentration, M

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Authors and Affiliations

  1. Department of Chemical Enzymology, Faculty of Chemistry, Lomonosov Moscow State University, 119899, Moscow, Russia

    Nikolay L. Eremeev, Alexandr V. Kukhtin, Eugenia A. Belyaeva & Novella F. Kazanskaya

Authors
  1. Nikolay L. Eremeev
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  2. Alexandr V. Kukhtin
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  3. Eugenia A. Belyaeva
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  4. Novella F. Kazanskaya
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Correspondence to Nikolay L. Eremeev.

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Eremeev, N.L., Kukhtin, A.V., Belyaeva, E.A. et al. Effect of thermosensitive matrix-phase transition on urease-catalyzed urea hydrolysis. Appl Biochem Biotechnol 76, 45–55 (1999). https://doi.org/10.1385/ABAB:76:1:45

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  • DOI: https://doi.org/10.1385/ABAB:76:1:45

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